This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ogierman, M. A. Articles by Manning, P. A. Search for Related Content PubMed PubMed Citation Articles by Ogierman, M. A. Articles by Manning, P. A.

 Previous Article  |  Next Article 

J. Bacteriol., Nov 1997, 7072-7080, Vol 179, No. 22
Copyright © 1997, American Society for Microbiology

Characterization of the Vibrio cholerae El Tor lipase operon lipAB and a protease gene downstream of the hly region

MA Ogierman, A Fallarino, T Riess, SG Williams, SR Attridge and PA Manning
Department of Microbiology and Immunology, University of Adelaide, South Australia.

We have cloned and sequenced a region encoding a lipase operon and a putative, previously uncharacterized metalloprotease of Vibrio cholerae O1. These lie downstream of hlyA and hlyB, which encode the El Tor hemolysin and methyl-accepting chemotactic factor, respectively. Previous reports identified the hlyC gene downstream of hlyAB, encoding an 18.3-kDa protein. However, we now show that this open reading frame (ORF) encodes a 33-kDa protein, and since the amino acid sequence is highly homologous to the triacylglyceride-specific lipase of Pseudomonas spp., hlyC has been renamed lipA. LipA contains the highly conserved pentapeptide and catalytic triad amino acid regions of the catalytic sites of other lipases. The region downstream of lipA has been sequenced and has revealed ORFs lipB and prtV. The amino acid sequence of lipB is homologous to those of the accessory lipase proteins (lipase-specific foldase) required by Pseudomonas and various other bacterial species for the production of mature active lipase, and in agreement with this, we show that both lipA and lipB are required to restore a lipase-deficient lipA null mutant of V. cholerae. The intergenic stop codon for lipA overlaps the ribosome-binding site for lipB, and a stem-loop resembling a rho-independent terminator is present immediately downstream from lipB, suggesting that lipA and lipB form a lipase operon in V. cholerae. prtV lies downstream of lipAB but is transcribed in the opposite direction and is predicted to share the same putative transcriptional terminator with lipAB. The zinc-binding and catalytic domains conserved among many metalloproteases are present in PrtV, which is highly homologous to the immune inhibitor A (InA) metalloprotease of Bacillus thuringiensis. PrtV was visualized as approximately 102 kDa, which is consistent with the coding capacity of the gene. The genetic organization of this region suggests that it is possibly part of a pathogenicity island, encoding products capable of damaging host cells and/or involved in nutrient acquisition by V. cholerae. However, neither lipA nor prtV null mutants were attenuated in the infant mouse model, nor did they exhibit reduced colonization potential compared with wild type in competition experiments.

This article has been cited by other articles:

• Varina, M., Denkin, S. M., Staroscik, A. M., Nelson, D. R. (2008). Identification and Characterization of Epp, the Secreted Processing Protease for the Vibrio anguillarum EmpA Metalloprotease. J. Bacteriol. 190: 6589-6597 [Abstract] [Full Text]  
• Bag, P. K., Bhowmik, P., Hajra, T. K., Ramamurthy, T., Sarkar, P., Majumder, M., Chowdhury, G., Das, S. C. (2008). Putative Virulence Traits and Pathogenicity of Vibrio cholerae Non-O1, Non-O139 Isolates from Surface Waters in Kolkata, India. Appl. Environ. Microbiol. 74: 5635-5644 [Abstract] [Full Text]  
• Vaitkevicius, K., Lindmark, B., Ou, G., Song, T., Toma, C., Iwanaga, M., Zhu, J., Andersson, A., Hammarstrom, M.-L., Tuck, S., Wai, S. N. (2006). A Vibrio cholerae protease needed for killing of Caenorhabditis elegans has a role in protection from natural predator grazing. Proc. Natl. Acad. Sci. USA 103: 9280-9285 [Abstract] [Full Text]  
• Rock, J. L., Nelson, D. R. (2006). Identification and Characterization of a Hemolysin Gene Cluster in Vibrio anguillarum.. Infect. Immun. 74: 2777-2786 [Abstract] [Full Text]  
• Mey, A. R., Wyckoff, E. E., Kanukurthy, V., Fisher, C. R., Payne, S. M. (2005). Iron and Fur Regulation in Vibrio cholerae and the Role of Fur in Virulence. Infect. Immun. 73: 8167-8178 [Abstract] [Full Text]  
• Mey, A. R., Wyckoff, E. E., Oglesby, A. G., Rab, E., Taylor, R. K., Payne, S. M. (2002). Identification of the Vibrio cholerae Enterobactin Receptors VctA and IrgA: IrgA Is Not Required for Virulence. Infect. Immun. 70: 3419-3426 [Abstract] [Full Text]  
• Fedhila, S., Nel, P., Lereclus, D. (2002). The InhA2 Metalloprotease of Bacillus thuringiensis Strain 407 Is Required for Pathogenicity in Insects Infected via the Oral Route. J. Bacteriol. 184: 3296-3304 [Abstract] [Full Text]  
• Grandvalet, C., Gominet, M., Lereclus, D. (2001). Identification of genes involved in the activation of the Bacillus thuringiensis inhA metalloprotease gene at the onset of sporulation. Microbiology 147: 1805-1813 [Abstract] [Full Text]  
• Drouault, S., Corthier, G., Ehrlich, S. D., Renault, P. (2000). Expression of the Staphylococcus hyicus Lipase in Lactococcus lactis. Appl. Environ. Microbiol. 66: 588-598 [Abstract] [Full Text]